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JXB Advance Access published online on January 27, 2009
Journal of Experimental Botany, doi:10.1093/jxb/ern346
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© 2009 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

RESEARCH PAPER

Trafficking of storage proteins in developing grain of wheat

Paola Tosi1,*, Mary Parker2, Cristina S. Gritsch1, Raffaella Carzaniga3, Barry Martin4 and Peter R. Shewry1

1Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, UK
2Institute of Food Research, Colney, Norwich NR4 7UA, UK
3Imperial College London, London SW7 2AZ, UK
4School of Life Sciences, Oxford Brookes University, Oxford OX3 0BP, UK

* To whom correspondence should be addressed: paola.tosi{at}bbsrc.ac.uk

The processing properties of the wheat flour are largely determined by the structures and interactions of the grain storage proteins (also called gluten proteins) which form a continuous visco-elastic network in dough. Wheat gluten proteins are classically divided into two groups, the monomeric gliadins and the polymeric glutenins, with the latter being further classified into low molecular weight (LMW) and high molecular weight (HMW) subunits. The synthesis, folding and deposition of the gluten proteins take place within the endomembrane system of the plant cell. However, determination of the precise routes of trafficking and deposition of individual gluten proteins in developing wheat grain has been limited in the past by the difficulty of developing monospecific antibodies. To overcome this limitation, a single gluten protein (a LMW subunit) was expressed in transgenic wheat with a C-terminal epitope tag, allowing the protein to be located in the cells of the developing grain using highly specific antibodies. This approach was also combined with the use of wider specificity antibodies to compare the trafficking and deposition of different gluten protein groups within the same endosperm cells. These studies are in agreement with previous suggestions that two trafficking pathways occur in wheat, with the proteins either being transported via the Golgi apparatus into the vacuole or accumulating directly within the lumen of the ER. They also suggest that the same individual protein could be trafficked by either pathway, possibly depending on the stage of development, and that segregation of gluten proteins both between and within protein bodies may occur.

Key words: Epitope tagging, gluten, immunolocalization, protein bodies, protein trafficking, wheat grain

Received 11 September 2008; Revised 5 December 2008 Accepted 5 December 2008


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